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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

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1437-4315
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Volume 386, Issue 8

Issues

The precursor of secreted aspartic proteinase Sapp1p from Candida parapsilosis can be activated both autocatalytically and by a membrane-bound processing proteinase

Jiří Dostál
  • Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, Prague 6, CZ-166 10, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Helena Dlouhá
  • Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, Prague 6, CZ-166 10, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Petr Maloň
  • Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, Prague 6, CZ-166 10, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Iva Pichová
  • Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, Prague 6, CZ-166 10, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Olga Hrušková-Heidingsfeldová
  • Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, Prague 6, CZ-166 10, Czech Republic
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2005-09-06 | DOI: https://doi.org/10.1515/BC.2005.093

Abstract

Opportunistic pathogens of the genus Candida produce secreted aspartic proteinases (Saps) that play an important role in virulence. Saps are synthesized as zymogens, but cell-free culture supernatants of Candida spp. contain only mature Saps. To study the zymogen conversion, the gene encoding a precursor of C. parapsilosis proteinase Sapp1p was cloned, expressed in E. coli and the product was purified. When placed in acidic conditions, the precursor was autocatalytically processed, yielding an active proteinase. The self-activation proceeded through an intermediate product and the resulting enzyme was one amino acid shorter than the authentic enzyme. This truncation did not cause changes in proteinase activity or secondary structure compared to the authentic Sapp1p. Accurate cleavage of the pro-mature junction, however, required a processing proteinase. A crude membrane fraction prepared from C. parapsilosis cells contained an enzyme with Kex2-like activity, which processed the Sapp1p precursor at the expected site. The pro-segment appeared to be indispensable for Sapp1p to attain an appropriate structure. When expressed without the pro-segment, the Sapp1p mature domain was not active and had a lower content of α-helical conformation, as measured by circular dichroism. A similar effect was observed when a His6-tag was linked to the C-terminus of Sapp1p or its precursor.

Keywords: aspartic proteinase; Candida parapsilosis; circular dichroism; His6-tag; zymogen conversion

About the article

Corresponding author


Received: March 1, 2005

Accepted: June 7, 2005

Published Online: 2005-09-06

Published in Print: 2005-08-01


Citation Information: Biological Chemistry, Volume 386, Issue 8, Pages 791–799, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2005.093.

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